SANS
data from solutions of
Human Splicing factor, proline- and glutamine-rich protein 5% SFPQ and 95% dSFPQ at a D2O matchpoint of 95%
in
150 mM KCl, 0.075% glycerol, 20 mM HEPES, 0.5 mM DTT,, pH 7.4
were collected
using a ORDELA/21000N detector
at a sample-detector distance of 1.3 m and
at a wavelength of λ = 0.6 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
at 25°C.
The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
SANS experiment indicating dimer partner exchange between deuterated and protiated monomers of full-length SFPQ. Contrast-matching has ensured signal is coming from protiated monomers of full-length SFPQ.
Additional details are available in the manuscript: Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation.
s, nm-1
